Abstract
The identification of a high-quality binding site and depiction of a target protein is of prime significance that leads to its functional annotations. In the present work, diverse binding site residues viz. Trp18, Asn44, Val46, Tyr73, Tyr77, Ala176, Glu178 were studied using SYBYL and it was envisaged that Tyr77 was conserved in family 11 xylanases. Furthermore, during residue conservation analysis through ConSurf method Tyr77 was observed as highly conserved among others. Molecular docking of endo-1, 4-beta xylanases (1YNA) with substrates viz. xylobiose and beta-D-xylopyranose established Tyr77 residue as conserved in both the binding sites and InterProScan analysis further verified Tyr77 in family 11 glycoside hydrolase motifs with a significantly good score of 1,604.
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Karthik, M.V.K., Shukla, P. (2012). Conclusion. In: Computational Strategies Towards Improved Protein Function Prophecy of Xylanases from Thermomyces lanuginosus. SpringerBriefs in Systems Biology. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-4723-8_5
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DOI: https://doi.org/10.1007/978-1-4614-4723-8_5
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